Allosteric Mechanisms of Signal Transduction

By Jean-Pierre Changeux, S. Edelstein. Science, 2005

694 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2ed944a1c24fdddc76697fd0ed5c04d314329931

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In Computational Theory and Mathematics

1. Debashish Chowdhury
2. Le Yan
3. Matthieu Wyart
4. Carolina Brito
5. Riccardo Ravasio

In Molecular Biology

1. Debashish Chowdhury
2. Qiang Cui
3. Martin Karplus
4. Eran Eyal
5. Lee-Wei Yang
6. Junseock Koh
7. Ivet Bahar
8. H. Youn

Citations in the corpus

• Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, background): “r r1 r([PaD] [PaLD] [PaL2D])/[D]total (4)”
• Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “Allostery is a mechanism for regulation of the structure, dynamics and function of an enzyme by the binding of another molecule, called effector, which can be a small molecule (a ligand) or another macromolecule [275, 276, 277, 278, 279, 280, 281, 282].”
• Dynamically driven protein allostery (2006, background): “According to the classical 'mechanical' view, allosteric interactions are mediated by a series of discrete conformational changes that alter protein structur”
• Global dynamics of proteins: bridging between structure and function. (2010, background): “In summary, increasing experimental and computational evidence supports the dominance of intrinsic, as opposed to induced, dynamics in controlling the conformational switches and allosteric signals of proteins (5, 10, 13, 22, 25, 70, 73); but the bound conformations understandably undergo further st”
• Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “Besides a mechanical view [30,31] of structural changes, the dynamics is also of interest in the allosteric regulation of protein activity.”
• On the accuracy of inferring energetic coupling between distant sites in protein families from evolutionary imprints: Illustrations using lattice model (2009, neutral): “tative pairs of sites (1,5), (2,6), (3,10), and (8,11) (Fig.”
• Nicotinic receptors: allosteric transitions and therapeutic targets in the nervous system (2009, background): “nicotinic receptor partial agonist: (1) binding and functional profile.”
• Architecture and coevolution of allosteric materials (2016, methodology): “Often, the activity of the main functional site depends on the binding of an effector on a distant site (1, 2).”
• Dynamical networks in tRNA:protein complexes (2009, background): “Such long distance coupling is at the very heart of allosteric regulation (3).”